Function and regulation of cullin–RING ubiquitin ligases

Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O ₂ -Regulated Prolyl Hydroxylation

Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535 · see citing works

HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O ₂ Sensing

Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · see citing works

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507 · see citing works

SKP1 Connects Cell Cycle Regulators to the Ubiquitin Proteolysis Machinery through a Novel Motif, the F-Box

Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M. G., Harper, J. W., & Elledge, S. J. (1996) · Cell · doi:10.1016/s0092-8674(00)80098-7 · Cited by 1,421 · see citing works

SCF and Cullin/RING H2-Based Ubiquitin Ligases

Deshaies, R. J. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.435 · Cited by 1,238 · see citing works

F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80403-1 · Cited by 1,227 · see citing works

The SCF ubiquitin ligase: insights into a molecular machine

Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114 · see citing works

Cyclin E-CDK2 is a regulator of p27Kip1.Preprint

Sheaff, R. J., Groudine, M. T., Gordon, M., Roberts, J., & Clurman, B. E. (1997) · Genes & Development · doi:10.1101/gad.11.11.1464 · Cited by 910 · see citing works

The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae

Schwob, É. (1994) · Cell · doi:10.1016/0092-8674(94)90193-7 · Cited by 886 · see citing works

A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.

Feldman, R. M. R., Correll, C. C., Kaplan, K. B., & Deshaies, R. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80404-3 · Cited by 872 · see citing works

Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function

Stebbins, C. E., Kaelin, W. G., & Pavletich, N. P. (1999) · Science · doi:10.1126/science.284.5413.455 · Cited by 852 · see citing works

Rbx1, a Component of the VHL Tumor Suppressor Complex and SCF Ubiquitin Ligase

Kamura, T., Koepp, D. M., Conrad, M. N., Skowyra, D., Moreland, R. J., Iliopoulos, O., Lane, W. S., Kaelin, W. G., Elledge, S. J., Conaway, R. C., et al. (1999) · Science · doi:10.1126/science.284.5414.657 · Cited by 786 · see citing works

Phosphorylation-Dependent Ubiquitination of Cyclin E by the SCF Fbw7 Ubiquitin Ligase

Koepp, D. M., Schaefer, L. K., Ye, X., Keyomarsi, K., Chu, C., Harper, J. W., & Elledge, S. J. (2001) · Science · doi:10.1126/science.1065203 · Cited by 764 · see citing works

Targeted disruption of Skp2 results in accumulation of cyclin E and p27Kip1, polyploidy and centrosome overduplication

Nakayama, K., Nagahama, H., Minamishima, Y. A., 雅記, 松., Nakamichi, I., Kitagawa, K., Shirane, M., Tsunematsu, R., Tsukiyama, T., Ishida, N., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.9.2069 · Cited by 719 · see citing works

Systematic analysis and nomenclature of mammalian F-box proteinsPreprint

Jin, J., Cardozo, T. J., Lovering, R. C., Elledge, S. J., Pagano, M., & Harper, J. W. (2004) · Genes & Development · doi:10.1101/gad.1255304 · Cited by 716 · see citing works

The ubiquitin ligase COP1 is a critical negative regulator of p53

Dornan, D., Wertz, I. E., Shimizu, H., Arnott, D. P., Frantz, G. D., Dowd, P., Rourke, K. O., Koeppen, H., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02514 · Cited by 700 · see citing works

Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome

Lyapina, S., Cope, G. A., Shevchenko, A., Serino, G., Tsuge, T., Zhou, C., Wolf, D. A., Wei, N., Shevchenko, A., & Deshaies, R. J. (2001) · Science · doi:10.1126/science.1059780 · Cited by 699 · see citing works

Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1

Cope, G. A., Suh, G. S. B., Aravind, L., Schwarz, S. E., Zipursky, S. L., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075901 · Cited by 682 · see citing works

Structure of a β-TrCP1-Skp1-β-Catenin Complex

Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612 · see citing works

Insights into SCF ubiquitin ligases from the structure of the Skp1–Skp2 complex

Schulman, B. A., Carrano, A. C., Jeffrey, P. D., Bowen, Z., Kinnucan, E., Finnin, M. S., Elledge, S. J., Harper, J. W., Pagano, M., & Pavletich, N. P. (2000) · Nature · doi:10.1038/35042620 · Cited by 610 · see citing works

Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formationPreprint

Montagnoli, A., FIORE, F., Eytan, E., Carrano, A. C., Draetta, G. F., Hershko, A., & Pagano, M. (1999) · Genes & Development · doi:10.1101/gad.13.9.1181 · Cited by 596 · see citing works

The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families

Kamura, T., Sato, S., Haque, D., Liu, L., Kaelin, W. G., Conaway, R. C., & Conaway, J. W. (1998) · Genes & Development · doi:10.1101/gad.12.24.3872 · Cited by 595 · see citing works

Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line

Strohmaier, H. M., Spruck, C., Kaiser, P., Won, K., Sangfelt, O., & Reed, S. I. (2001) · Nature · doi:10.1038/35095076 · Cited by 584 · see citing works

Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase

Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 510 · see citing works

Skp2 Regulates Myc Protein Stability and Activity

Kim, S. Y., Herbst, A., Tworkowski, K. A., Salghetti, S. E., & Tansey, W. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00173-4 · Cited by 508 · see citing works

Control of the SCFSkp2–Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase

Bashir, T., Dorrello, N. V., Amador, V., Guardavaccaro, D., & Pagano, M. (2004) · Nature · doi:10.1038/nature02330 · Cited by 504 · see citing works

Chemical Genetic Control of Protein Levels: Selective in Vivo Targeted Degradation

Schneekloth, J. S., Fonseca, F. N., Koldobskiy, M. A., Mandal, A., Deshaies, R. J., Sakamoto, K. M., & Crews, C. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039025z · Cited by 502 · see citing works

BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3

Xu, L., Yue, W., Reboul, J., Vaglio, P., Shin, T.-H., Vidal, M., Elledge, S. J., & Harper, J. W. (2003) · Nature · doi:10.1038/nature01985 · Cited by 497 · see citing works

Assembly of cyclin D-dependent kinase and titration of p27 ^Kip1 regulated by mitogen-activated protein kinase kinase (MEK1)

Cheng, M., Sexl, V., Sherr, C. J., & Roussel, M. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.1091 · Cited by 496 · see citing works

Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex

Wei, W., Ayad, N. G., Wan, Y., Zhang, G.-J., Kirschner, M. W., & Kaelin, W. G. (2004) · Nature · doi:10.1038/nature02381 · Cited by 495 · see citing works

HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis

Takahashi, A., Casais, C., Ichimura, K., & Shirasu, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2033934100 · Cited by 494 · see citing works

Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation.Preprint

Clurman, B. E., Sheaff, R. J., Thress, K. S., Groudine, M. T., & Roberts, J. M. (1996) · Genes & Development · doi:10.1101/gad.10.16.1979 · Cited by 488 · see citing works

Interactions of the COP9 Signalosome with the E3 Ubiquitin Ligase SCF TIR1 in Mediating Auxin Response

Schwechheimer, C., Serino, G., Callis, J., Crosby, W. L., Lyapina, S., Deshaies, R. J., Gray, W. M., Estelle, M. A., & Deng, X. (2001) · Science · doi:10.1126/science.1059776 · Cited by 475 · see citing works

The F-Box Protein Skp2 Participates in c-Myc Proteosomal Degradation and Acts as a Cofactor for c-Myc-Regulated Transcription

von der Lehr, N., Johansson, S. M., Wu, S., Bahram, F., Castell, A., Cetinkaya, C., Hydbring, P., Weidung, I., Nakayama, K., Nakayama, K., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00193-x · Cited by 475 · see citing works

The cell-cycle regulatory protein Cks1 is required for SCFSkp2-mediated ubiquitinylation of p27

Ganoth, D., Bornstein, G., Ko, T. K., Larsen, B. G., Tyers, M., Pagano, M., & Hershko, A. (2001) · Nature Cell Biology · doi:10.1038/35060126 · Cited by 468 · see citing works

ROC1, a Homolog of APC11, Represents a Family of Cullin Partners with an Associated Ubiquitin Ligase Activity

Ohta, T., Michel, J. J. C., Schottelius, A. J. G., & Xiong, Y. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80482-7 · Cited by 461 · see citing works

Targeting of protein ubiquitination by BTB–Cullin 3–Roc1 ubiquitin ligases

Furukawa, M., He, Y. J., Borchers, C. H., & Xiong, Y. (2003) · Nature Cell Biology · doi:10.1038/ncb1056 · Cited by 459 · see citing works

Phosphorylation of Sic1p by G 1 Cdk Required for Its Degradation and Entry into S Phase

Verma, R., Annan, R. S., Huddleston, M. J., Carr, S. A., Reynard, G. J., & Deshaies, R. J. (1997) · Science · doi:10.1126/science.278.5337.455 · Cited by 449 · see citing works

The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase

Pintard, L., Willis, J. H., Willems, A. R., Johnson, J.-L., Srayko, M., Kurz, T., Luke-Glaser, S., Mains, P. E., Tyers, M., Bowerman, B. A., et al. (2003) · Nature · doi:10.1038/nature01959 · Cited by 431 · see citing works

Cullin‐based ubiquitin ligases: Cul3–BTB complexes join the family

Pintard, L., Willems, A. R., & Peter, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600186 · Cited by 413 · see citing works

COP9 Signalosome

Cope, G. A., & Deshaies, R. J. (2003) · Cell · doi:10.1016/s0092-8674(03)00722-0 · Cited by 409 · see citing works

Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cellsPreprint

Singer, J. D., Gurian-West, M., Clurman, B. E., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.18.2375 · Cited by 404 · see citing works

Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34Preprint

Seol, J. H., Feldman, R. M. R., Zachariae, W., Shevchenko, A., Correll, C. C., Lyapina, S., Chi, Y., Gálová, M., Claypool, J. T., Sandmeyer, S. B., et al. (1999) · Genes & Development · doi:10.1101/gad.13.12.1614 · Cited by 403 · see citing works

Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein

Hubert, D. A., Tornero, P., Belkhadir, Y., Krishna, P., Takahashi, A., Shirasu, K., & Dangl, J. L. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg547 · Cited by 398 · see citing works

SGT1 Encodes an Essential Component of the Yeast Kinetochore Assembly Pathway and a Novel Subunit of the SCF Ubiquitin Ligase Complex

Kitagawa, K., Skowyra, D., Elledge, S. J., Harper, J. W., & Hieter, P. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80184-7 · Cited by 387 · see citing works

Parkin Is a Component of an SCF-like Ubiquitin Ligase Complex and Protects Postmitotic Neurons from Kainate Excitotoxicity

Staropoli, J. F., McDermott, C., Martinat, C., Schulman, B. A., Demireva, E. Y., & Abeliovich, A. (2003) · Neuron · doi:10.1016/s0896-6273(03)00084-9 · Cited by 378 · see citing works

Reconstitution of G 1 Cyclin Ubiquitination with Complexes Containing SCF Grr1 and Rbx1

Skowyra, D., Koepp, D. M., Kamura, T., Conrad, M. N., Conaway, R. C., Conaway, J. W., Elledge, S. J., & Harper, J. W. (1999) · Science · doi:10.1126/science.284.5414.662 · Cited by 377 · see citing works

Human De-Etiolated-1 Regulates c-Jun by Assembling a CUL4A Ubiquitin Ligase

Wertz, I. E., O’Rourke, K. M., Zhang, Z., Dornan, D., Arnott, D. P., Deshaies, R. J., & Dixit, V. M. (2004) · Science · doi:10.1126/science.1093549 · Cited by 366 · see citing works

Multisite Phosphorylation by Cdk2 and GSK3 Controls Cyclin E Degradation

Welcker, M., Singer, J. D., Loeb, K. R., Grim, J. A., Bloecher, A., Gurian-West, M., Clurman, B. E., & Roberts, J. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00287-9 · Cited by 364 · see citing works

Nedd8 Modification of Cul-1 Activates SCF^βTrCP-Dependent Ubiquitination of IκBα

Read, M. A., Brownell, J. E., Gladysheva, T. B., Hottelet, M., Parent, L. A., Coggins, M. B., Pierce, J. W., Podust, V. N., Luo, R.-S., Chau, V., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2326-2333.2000 · Cited by 363 · see citing works

A novel protein modification pathway related to the ubiquitin system

Liakopoulos, D., Doenges, G., Matuschewski, K., & Jentsch, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.8.2208 · Cited by 361 · see citing works

Activation of cyclin E/CDK2 is coupled to site‐specific autophosphorylation and ubiquitin‐dependent degradation of cyclin E.

Won, K. A., & Reed, S. I. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00793.x · Cited by 360 · see citing works

Regulation of Transcriptional Activation Domain Function by Ubiquitin

Salghetti, S. E., Caudy, A. A., Chenoweth, J. G., & Tansey, W. P. (2001) · Science · doi:10.1126/science.1062079 · Cited by 356 · see citing works

Parc

Nikolaev, A. Y., Li, M., Puskas, N., Qin, J., & Gu, W. J. (2003) · Cell · doi:10.1016/s0092-8674(02)01255-2 · Cited by 355 · see citing works

A CDK-Independent Function of Mammalian Cks1

Spruck, C., Strohmaier, H. M., Watson, M. H., Smith, A. P. L., Ryan, A., Krek, W., & Reed, S. I. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00210-6 · Cited by 355 · see citing works

Control of Meiotic and Mitotic Progression by the F Box Protein β-Trcp1 In Vivo

Guardavaccaro, D., Kudo, Y., Boulaire, J., Barchi, M., Busino, L., Donzelli, M., Margottin-Goguet, F., Jackson, P. K., Yamasaki, L., & Pagano, M. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00154-0 · Cited by 355 · see citing works

E3 ubiquitin ligase that recognizes sugar chains

Yoshida, Y., Chiba, T., Tokunaga, F., Kawasaki, H., Iwaï, K., Suzuki, T., Ito, Y., Matsuoka, K., Yoshida, M., Tanaka, K., et al. (2002) · Nature · doi:10.1038/nature00890 · Cited by 351 · see citing works

Recruitment of a ROC1–CUL1 Ubiquitin Ligase by Skp1 and HOS to Catalyze the Ubiquitination of IκBα

Tan, P., Fuchs, S. Y., Chen, A., Wu, K. K.-Y., Gomez, C., Ronai, Z. A., & Pan, Z. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80481-5 · Cited by 345 · see citing works

NEDD8 recruits E2‐ubiquitin to SCF E3 ligase

Kawakami, T., Chiba, T., Suzuki, T., Iwai, K., Yamanaka, K., Minato, N., Suzuki, H., Shimbara, N., Hidaka, Y., Osaka, F., et al. (2001) · EMBO Journal · doi:10.1093/emboj/20.15.4003 · Cited by 344 · see citing works

BTB/POZ Domain Proteins Are Putative Substrate Adaptors for Cullin 3 Ubiquitin Ligases

Geyer, R. K., Wee, S., Anderson, S., Yates, J. R., & Wolf, D. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00341-1 · Cited by 339 · see citing works

The Ubiquitin Ligase SCF Fbw7 Antagonizes Apoptotic JNK Signaling

Nateri, A. S., Riera-Sans, L., Costa, C. D., & Behrens, A. (2004) · Science · doi:10.1126/science.1092880 · Cited by 339 · see citing works

Prophase Destruction of Emi1 by the SCFβTrCP/Slimb Ubiquitin Ligase Activates the Anaphase Promoting Complex to Allow Progression beyond Prometaphase

Margottin-Goguet, F., Hsu, J. Y., Loktev, A. V., Hsieh, H.-M., Reimann, J. D. R., & Jackson, P. K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00153-9 · Cited by 337 · see citing works

Mass Spectrometric Analysis of the Anaphase-Promoting Complex from Yeast: Identification of a Subunit Related to Cullins

Zachariae, W., Shevchenko, A., Andrews, P. D., Ciosk, R., Gálová, M., Stark, M. J. R., Mann, M., & Nasmyth, K. (1998) · Science · doi:10.1126/science.279.5354.1216 · Cited by 326 · see citing works

NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases

Liu, J., Furukawa, M., Matsumoto, T., & Xiong, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00783-9 · Cited by 319 · see citing works

Modification of yeast Cdc53p by the ubiquitin-related protein Rub1p affects function of the SCFCdc4 complexPreprint

Lammer, D., Mathias, N., Laplaza, J. M., Jiang, W., Liu, Y., Callis, J., Goebl, M. G., & Estelle, M. A. (1998) · Genes & Development · doi:10.1101/gad.12.7.914 · Cited by 312 · see citing works

CAND1 Binds to Unneddylated CUL1 and Regulates the Formation of SCF Ubiquitin E3 Ligase Complex

Zheng, J., Yang, X., Harrell, J. M., Ryzhikov, S., Shim, E., Lykke‐Hartmann, K., Wei, N., Sun, H., Kobayashi, R., & Zhang, H. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00784-0 · Cited by 309 · see citing works

Negative regulation of Gcn4 and Msn2 transcription factors by Srb10 cyclin-dependent kinasePreprint

Chi, Y., Huddleston, M. J., Zhang, X., Young, R. A., Annan, R. S., Carr, S. A., & Deshaies, R. J. (2001) · Genes & Development · doi:10.1101/gad.867501 · Cited by 303 · see citing works

Regulation of Transcription by Ubiquitination without Proteolysis

Kaiser, P., Flick, K. M., Wittenberg, C., & Reed, S. I. (2000) · Cell · doi:10.1016/s0092-8674(00)00036-2 · Cited by 292 · see citing works

Covalent modification of all members of human cullin family proteins by NEDD8

Hori, T., Osaka, F., Chiba, T., Miyamoto, C., Okabayashi, K., Shimbara, N., Kato, S., & Tanaka, K. (1999) · Oncogene · doi:10.1038/sj.onc.1203093 · Cited by 291 · see citing works

Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover

Reed, S. I. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1246 · Cited by 280 · see citing works

The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2Preprint

Kamura, T., Conrad, M. N., Yan, Q., Conaway, R. C., & Conaway, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.22.2928 · Cited by 270 · see citing works

Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism

Galan, J., & Peter, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9124 · Cited by 269 · see citing works

Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly

Seol, J. H., Shevchenko, A., Shevchenko, A., & Deshaies, R. J. (2001) · Nature Cell Biology · doi:10.1038/35070067 · Cited by 263 · see citing works

Ubiquitination and Degradation of the Substrate Recognition Subunits of SCF Ubiquitin–Protein Ligases

Zhou, P., & Howley, P. M. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80156-2 · Cited by 259 · see citing works

JAMM: A Metalloprotease-Like Zinc Site in the Proteasome and Signalosome

Ambroggio, X. I., Rees, D. C., & Deshaies, R. J. (2003) · PLoS Biology · doi:10.1371/journal.pbio.0020002 · Cited by 248 · see citing works

Identification of a Cullin Homology Region in a Subunit of the Anaphase-Promoting Complex

Yu, H., Peters, J., King, R. W., Page, A. M., Hieter, P., & Kirschner, M. W. (1998) · Science · doi:10.1126/science.279.5354.1219 · Cited by 248 · see citing works

A Nedd8 conjugation pathway is essential for proteolytic targeting of p27 Kip1 by ubiquitination

Podust, V. N., Brownell, J. E., Gladysheva, T. B., Luo, R.-S., Wang, C., Coggins, M. B., Pierce, J. W., Lightcap, E. S., & Chau, V. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.090465597 · Cited by 244 · see citing works

An SCF-like ubiquitin ligase complex that controls presynaptic differentiation

Liao, E. H., Hung, W., Abrams, B. S., & Zhen, M. (2004) · Nature · doi:10.1038/nature02647 · Cited by 233 · see citing works

Rapid Degradation of the G 1 Cyclin Cln2 Induced by CDK-Dependent Phosphorylation

Lanker, S., Valdivieso, M. ‐., & Wittenberg, C. (1996) · Science · doi:10.1126/science.271.5255.1597 · Cited by 232 · see citing works

The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice

Tateishi, K., Omata, M., Tanaka, K., & Chiba, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104035 · Cited by 230 · see citing works

Paramyxoviruses SV5 and HPIV2 Assemble STAT Protein Ubiquitin Ligase Complexes from Cellular Components

Ulane, C. M., & Horvath, C. M. (2002) · Virology · doi:10.1006/viro.2002.1773 · Cited by 225 · see citing works

Covalent modifier NEDD8 is essential for SCF ubiquitin‐ligase in fission yeast

Osaka, F., Saeki, M., Katayama, S., Aida, N., Toh‐e, A., Kominami, K., Toda, T., Suzuki, T., Chiba, T., Tanaka, K., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3475 · Cited by 217 · see citing works

Conjugation of Nedd8 to CUL1 Enhances the Ability of the ROC1-CUL1 Complex to Promote Ubiquitin Polymerization

Wu, K. K.-Y., Chen, A., & Pan, Z. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004847200 · Cited by 204 · see citing works

Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanismsPreprint

Liu, C., Powell, K. A., Mundt, K., Wu, L., Carr, A. M., & Caspari, T. (2003) · Genes & Development · doi:10.1101/gad.1090803 · Cited by 191 · see citing works

Distinct protein degradation mechanisms mediated by Cul1 and Cul3 controlling Ci stability in Drosophila eye developmentPreprint

Ou, C.-Y., Lin, Y., Chen, Y., et al. (2002) · Genes & Development · doi:10.1101/gad.1011402 · Cited by 188 · see citing works

Fission Yeast COP9/Signalosome Suppresses Cullin Activity through Recruitment of the Deubiquitylating Enzyme Ubp12p

Zhou, C., Wee, S., Rhee, E., Naumann, M., Dubiel, W., & Wolf, D. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00136-9 · Cited by 180 · see citing works

Skp1p and the F-Box Protein Rcy1p Form a Non-SCF Complex Involved in Recycling of the SNARE Snc1p in Yeast

Galan, J., Wiederkehr, A., Seol, J. H., Haguenauer‐Tsapis, R., Deshaies, R. J., Riezman, H., & Peter, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.9.3105-3117.2001 · Cited by 180 · see citing works

Tome-1, a Trigger of Mitotic Entry, Is Degraded during G1 via the APC

Ayad, N. G., Rankin, S., Murakami, M. S., Jebanathirajah, J. A., Gygi, S. P., & Kirschner, M. W. (2003) · Cell · doi:10.1016/s0092-8674(03)00232-0 · Cited by 179 · see citing works

Neddylation and Deneddylation of CUL-3 Is Required to Target MEI-1/Katanin for Degradation at the Meiosis-to-Mitosis Transition in C. elegans

Pintard, L., Kurz, T., Luke-Glaser, S., Willis, J. H., Peter, M., & Bowerman, B. A. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00336-1 · Cited by 178 · see citing works

An intact NEDD8 pathway is required for Cullin‐dependent ubiquitylation in mammalian cells

Ohh, M., Kim, W. Y., Moslehi, J. J., Chen, Y., Chau, V., Read, M. A., & Kaelin, W. G. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf028 · Cited by 177 · see citing works

CUL7: A DOC domain-containing cullin selectively binds Skp1⋅Fbx29 to form an SCF-like complex

Dias, D. C., Dolios, G., Wang, R., & Pan, Z. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252646399 · Cited by 165 · see citing works

Proteolysis-independent regulation of the transcription factor Met4 by a single Lys 48-linked ubiquitin chain

Flick, K. M., Ouni, I., Wohlschlegel, J. A., Capati, C., McDonald, W. H., Yates, J. R., & Kaiser, P. (2004) · Nature Cell Biology · doi:10.1038/ncb1143 · Cited by 162 · see citing works

Cullin 4A Associates with the UV-damaged DNA-binding Protein DDB

Shiyanov, P. A., Nag, A., & Raychaudhuri, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35309 · Cited by 159 · see citing works

Context of Multiubiquitin Chain Attachment Influences the Rate of Sic1 Degradation

Petroski, M. D., & Deshaies, R. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00221-1 · Cited by 149 · see citing works

Genetic Evidence for the Essential Role of β-Transducin Repeat-containing Protein in the Inducible Processing of NF-κB2/p100

Fong, A., & Sun, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200151200 · Cited by 144 · see citing works

Regulating the Yeast Kinetochore by Ubiquitin-Dependent Degradation and Skp1p-Mediated Phosphorylation

Kaplan, K. B., Hyman, A. A., & Sorger, P. K. (1997) · Cell · doi:10.1016/s0092-8674(00)80435-3 · Cited by 142 · see citing works

Cdc34 and the F-box protein Met30 are required for degradation of the Cdk-inhibitory kinase Swe1Preprint

Kaiser, P., Sia, R. A. L., Bardes, E. S. G., Lew, D. J., & Reed, S. I. (1998) · Genes & Development · doi:10.1101/gad.12.16.2587 · Cited by 141 · see citing works

Arabidopsis CAND1, an Unmodified CUL1-Interacting Protein, Is Involved in Multiple Developmental Pathways Controlled by Ubiquitin/Proteasome-Mediated Protein Degradation

Feng, S., Shen, Y., Sullivan, J. A., Rubio, V., Xiong, Y., Sun, T., & Deng, X. W. (2004) · The Plant Cell · doi:10.1105/tpc.021949 · Cited by 137 · see citing works

Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products

Schoenfeld, A. R., Davidowitz, E. J., & Burk, R. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.15.8507 · Cited by 135 · see citing works

Homodimer of Two F-box Proteins βTrCP1 or βTrCP2 Binds to IκBα for Signal-dependent Ubiquitination

Suzuki, H., Chiba, T., Suzuki, T., Fujita, T., Ikenoue, T., Omata, M., Furuichi, K., Shikama, H., & Tanaka, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2877 · Cited by 131 · see citing works

Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A.

Michel, J. J. C., & Xiong, Y. (1998) · PubMed · Cited by 126 · see citing works

Degradation of the Transcription Factor Gcn4 Requires the Kinase Pho85 and the SCFCDC4Ubiquitin–Ligase Complex

Meimoun, A., Holtzman, T., Weissman, Z., McBride, H. J., Stillman, D. J., Fink, G. R., & Kornitzer, D. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.3.915 · Cited by 126 · see citing works

Structure of the Jab1/MPN Domain and Its Implications for Proteasome Function

Tran, H. J. T. T., Allen, M. D., Löwe, J., & Bycroft, M. (2003) · Biochemistry · doi:10.1021/bi035033g · Cited by 125 · see citing works

Dual Regulation of the Met4 Transcription Factor by Ubiquitin-Dependent Degradation and Inhibition of Promoter Recruitment

Kuras, L., Rouillon, A., Lee, T., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00561-0 · Cited by 124 · see citing works

The COP9 Signalosome Promotes Degradation of Cyclin E during Early Drosophila Oogenesis

Doronkin, S., Djagaeva, I., & Beckendorf, S. K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00121-7 · Cited by 121 · see citing works

Pseudosubstrate regulation of the SCF β-TrCP ubiquitin ligase by hnRNP-UPreprint

Davis, M., Hatzubai, A., Andersen, J., Ben-Shushan, E., Fisher, G. Z., Yaron, A., Bauskin, A. R., Mercurio, F., Mann, M., & Ben‐Neriah, Y. (2002) · Genes & Development · doi:10.1101/gad.218702 · Cited by 119 · see citing works

The Unstable F-box Protein p58-Ctf13 Forms the Structural Core of the CBF3 Kinetochore Complex

Russell, I., Grancell, A. S., & Sorger, P. K. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.5.933 · Cited by 115 · see citing works

Nuclear‐specific degradation of Far1 is controlled by the localization of the F‐box protein Cdc4

Blondel, M., Galan, J., Chi, Y., Lafourcade, C., Longaretti, C., Deshaies, R. J., & Peter, M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.6085 · Cited by 110 · see citing works

Arabidopsis ETA2 , an Apparent Ortholog of the Human Cullin-Interacting Protein CAND1, Is Required for Auxin Responses Mediated by the SCF TIR1 Ubiquitin Ligase

Chuang, H.-W., Zhang, W., & Gray, W. M. (2004) · The Plant Cell · doi:10.1105/tpc.021923 · Cited by 110 · see citing works

Targeted Proteomic Study of the Cyclin-Cdk Module

Archambault, V., Chang, E. J., Drapkin, B. J., Cross, F. R., Chait, B. T., & Rout, M. P. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.05.025 · Cited by 109 · see citing works

AtCAND1, A HEAT-Repeat Protein That Participates in Auxin Signaling in Arabidopsis

Cheng, Y., Dai, X., & Zhao, Y. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.044495 · Cited by 107 · see citing works

Selective Degradation of Ubiquitinated Sic1 by Purified 26S Proteasome Yields Active S Phase Cyclin-Cdk

Verma, R., McDonald, W. H., Yates, J. R., & Deshaies, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00308-2 · Cited by 103 · see citing works

Mathematical Modeling Suggests Cooperative Interactions between a Disordered Polyvalent Ligand and a Single Receptor Site

Klein, P., Pawson, T. J., & Tyers, M. (2003) · Current Biology · doi:10.1016/j.cub.2003.09.027 · Cited by 96 · see citing works

When protein destruction runs amok, malignancy is on the loose

Pagano, M., & Benmaamar, R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00243-5 · Cited by 90 · see citing works

Activation of UBC5 Ubiquitin-conjugating Enzyme by the RING Finger of ROC1 and Assembly of Active Ubiquitin Ligases by All Cullins

Furukawa, M., Ohta, T., & Xiong, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108565200 · Cited by 83 · see citing works

Regulation of the Transcription Factor Gcn4 by Pho85 Cyclin Pcl5

Shemer, R., Meimoun, A., Holtzman, T., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5395-5404.2002 · Cited by 83 · see citing works

Oncogenic aberrations of cullin-dependent ubiquitin ligases

Guardavaccaro, D., & Pagano, M. (2004) · Oncogene · doi:10.1038/sj.onc.1207413 · Cited by 82 · see citing works

Release of Ubiquitin-Charged Cdc34-S∼Ub from the RING Domain Is Essential for Ubiquitination of the SCFCdc4-Bound Substrate Sic1

Deffenbaugh, A. E., Scaglione, K. M., Zhang, L., Moore, J. M., Buranda, T., Sklar, L. A., & Skowyra, D. (2003) · Cell · doi:10.1016/s0092-8674(03)00641-x · Cited by 79 · see citing works

A protein knockdown strategy to study the function of β-catenin in tumorigenesis

Cong, F., Zhang, J., Pao, W. J., Zhou, P., & VARMUS, H. E. (2003) · BMC Molecular Biology · doi:10.1186/1471-2199-4-10 · Cited by 75 · see citing works

Triggering ubiquitination of a CDK inhibitor at origins of DNA replication

Furstenthal, L., Swanson, C. A., Kaiser, B. K., et al. (2001) · Nature Cell Biology · doi:10.1038/35087026 · Cited by 72 · see citing works

Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro

Kus, B., Caldon, C. E., Andorn‐Broza, R., & Edwards, A. M. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10620 · Cited by 72 · see citing works

TIP120A Associates with Cullins and Modulates Ubiquitin Ligase Activity

Min, K.-W., Hwang, J., Lee, J., Park, Y., Tamura, T.-A., & Yoon, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213070200 · Cited by 72 · see citing works

Stability of Homologue of Slimb F-box Protein Is Regulated by Availability of Its Substrate

Li, Y., Gazdoiu, S., Pan, Z., & Fuchs, S. Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312301200 · Cited by 70 · see citing works

Drosophila Roc1a Encodes a RING-H2 Protein with a Unique Function in Processing the Hh Signal Transducer Ci by the SCF E3 Ubiquitin Ligase

Noureddine, M., Donaldson, T. D., Thacker, S. A., & Duronio, R. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00164-8 · Cited by 65 · see citing works

Preferential interaction of TIP120A with Cul1 that is not modified by NEDD8 and not associated with Skp1

Oshikawa, K., Matsumoto, M., Yada, M., Kamura, T., Hatakeyama, S., & Nakayama, K. I. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00501-1 · Cited by 63 · see citing works

Functional and physical characterization of the cell cycle ubiquitin-conjugating enzyme CDC34 (UBC3). Identification of a functional determinant within the tail that facilitates CDC34 self-association

Ptak, C. P., Prendergast, J. A., Hodgins, R., et al. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47228-6 · Cited by 61 · see citing works

An Essential Domain within Cdc34p Is Required for Binding to a Complex Containing Cdc4p and Cdc53p in Saccharomyces cerevisiae

Mathias, N., Steussy, C. N., & Goebl, M. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.7.4040 · Cited by 59 · see citing works

Cdc34 Self-Association Is Facilitated by Ubiquitin Thiolester Formation and Is Required for Its Catalytic Activity

Varelas, X., Ptak, C. P., & Ellison, M. J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5388-5400.2003 · Cited by 52 · see citing works

Exploring the functional complexity of cellular proteins by protein knockout

Zhang, J., Zheng, N., & Zhou, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2233012100 · Cited by 51 · see citing works

Encore facilitates SCF-Ubiquitin-proteasome-dependent proteolysis duringDrosophilaoogenesis

Ohlmeyer, J. T., & Schüpbach, T. (2003) · Development · doi:10.1242/dev.00855 · Cited by 47 · see citing works

Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4

Jäger, S., Strayle, J., Heinemeyer, W., & Wolf, D. H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4423 · Cited by 45 · see citing works

Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop1p and Pop2p

Seibert, V., Prohl, C., Schoultz, I., et al. (2002) · BMC Biochemistry · doi:10.1186/1471-2091-3-22 · Cited by 42 · see citing works

SCFβ-TRCP and phosphorylation dependent ubiquitination of IκBα catalyzed by Ubc3 and Ubc4

Strack, P. R., Caligiuri, M., Pelletier, M., et al. (2000) · Oncogene · doi:10.1038/sj.onc.1203647 · Cited by 41 · see citing works

SCFhFBH1 can act as helicase and E3 ubiquitin ligase

Kim, J., & Kim, J.-H. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh534 · Cited by 40 · see citing works

DNA Damage Response-mediated Degradation of Ho Endonuclease via the Ubiquitin System Involves Its Nuclear Export

Kaplun, L., Ivantsiv, Y., Bakhrat, A., & Raveh, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308671200 · Cited by 39 · see citing works

Degrading Ci: who is Cul-pable?Preprint

Jiang, J. (2002) · Genes & Development · doi:10.1101/gad.1027902 · Cited by 36 · see citing works

TIP120A associates with unneddylated cullin 1 and regulates its neddylation

Hwang, J., Min, K.-W., Tamura, T.-A., & Yoon, J. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00321-1 · Cited by 35 · see citing works

Intragenic Suppression among CDC34 ( UBC3 ) Mutations Defines a Class of Ubiquitin-Conjugating Catalytic Domains

Liu, Y., Mathias, N., Steussy, C. N., et al. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.10.5635 · Cited by 35 · see citing works

Overproduction of Polypeptides Corresponding to the Amino Terminus of the F-Box Proteins Cdc4p and Met30p Inhibits Ubiquitin Ligase Activities of Their SCF Complexes

Dixon, C., Brunson, L. E., Roy, M. M., Smothers, D. B., Sehorn, M. G., & Mathias, N. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.1.123-133.2003 · Cited by 22 · see citing works

Creation of a Pluripotent Ubiquitin-Conjugating Enzyme

Ptak, C. P., Gwozd, C., Huzil, J. T., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.19.6537-6548.2001 · Cited by 19 · see citing works

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679 · see citing works

Identification of a Primary Target of Thalidomide Teratogenicity

Ito, T., Ando, H., Suzuki, T., Ogura, T., Hotta, K., Imamura, Y., Yamaguchi, Y., & Handa, H. (2010) · Science · doi:10.1126/science.1177319 · Cited by 2,136 · see citing works

An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer

Soucy, T. A., Smith, P. G., Milhollen, M. A., Berger, A. J., Gavin, J. M., Adhikari, S., Brownell, J. E., Burke, K. E., Cardin, D. P., Critchley, S., et al. (2009) · Nature · doi:10.1038/nature07884 · Cited by 1,990 · see citing works

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818 · see citing works

Phthalimide conjugation as a strategy for in vivo target protein degradation

Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., & Bradner, J. E. (2015) · Science · doi:10.1126/science.aab1433 · Cited by 1,760 · see citing works

Mechanism of auxin perception by the TIR1 ubiquitin ligase

Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688 · see citing works

Induced protein degradation: an emerging drug discovery paradigm

Lai, A. C., & Crews, C. M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.211 · Cited by 1,486 · see citing works

The anaphase promoting complex/cyclosome: a machine designed to destroy

Peters, J.-M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1988 · Cited by 1,315 · see citing works

Protein degradation by the ubiquitin-proteasome pathway in normal and disease states

Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234 · see citing works

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works

Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15

Han, T., Goralski, M., Gaskill, N., Capota, E., Kim, J., Ting, T. C., Xie, Y., Williams, N. S., & Nijhawan, D. (2017) · Science · doi:10.1126/science.aal3755 · Cited by 762 · see citing works

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation

Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767 · see citing works

Keap1 Recruits Neh2 through Binding to ETGE and DLG Motifs: Characterization of the Two-Site Molecular Recognition Model

Tong, K. I., Katoh, Y., Kusunoki, H., Itoh, K., Tanaka, T., & Yamamoto, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2887-2900.2006 · Cited by 759 · see citing works

The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle

Clarke, B. A., Drujan, D., Willis, M. S., Murphy, L. O., Corpina, R. A., Burova, E., Rakhilin, S. V., Stitt, T. N., Patterson, C., Latres, E., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.009 · Cited by 683 · see citing works

Molecular architecture and assembly of the DDB1–CUL4A ubiquitin ligase machinery

Angers, S., Li, T., Yi, X., MacCoss, M. J., Moon, R. T., & Zheng, N. (2006) · Nature · doi:10.1038/nature05175 · Cited by 674 · see citing works

A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1

Jin, J., Arias, E. E., Chen, J., Harper, J. W., & Walter, J. C. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.010 · Cited by 632 · see citing works

Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity

Chowdhry, S., Zhang, Y., McMahon, M., Sutherland, C., Cuadrado, A., & Hayes, J. D. (2013) · Oncogene · doi:10.1038/onc.2012.388 · Cited by 657 · see citing works

Mammalian iron metabolism and its control by iron regulatory proteins

Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works

Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases

Zhuang, M., Calabrese, M. F., Liu, J., Waddell, M. B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.022 · Cited by 486 · see citing works

Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism

Tong, K. I., Kobayashi, A., Katsuoka, F., & Yamamoto, M. (2006) · Biological Chemistry · doi:10.1515/bc.2006.164 · Cited by 473 · see citing works

MYC degradation

Farrell, A. S., & Sears, R. C. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014365 · Cited by 468 · see citing works

DCAFs, the Missing Link of the CUL4-DDB1 Ubiquitin Ligase

Lee, J., & Zhou, P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.001 · Cited by 460 · see citing works

Control of iron homeostasis by an iron-regulated ubiquitin ligase

Vashisht, A. A., Zumbrennen, K. B., Huang, X., Powers, D. N., Durazo, A., Sun, D., Bhaskaran, N., Persson, A., Uhlen, M., Sangfelt, O., et al. (2009) · Science · doi:10.1126/science.1176333 · Cited by 429 · see citing works

Rational discovery of molecular glue degraders via scalable chemical profiling

Mayor-Ruiz, C., Bauer, S., Brand, M., Kozicka, Z., Siklos, M., Imrichova, H., Kaltheuner, I. H., Hahn, E., Seiler, K., Koren, A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0594-x · Cited by 369 · see citing works

The KLHL12–Cullin-3 ubiquitin ligase negatively regulates the Wnt–β-catenin pathway by targeting Dishevelled for degradation

Angers, S., Thorpe, C. J., Biechele, T. L., Goldenberg, S. J., Zheng, N., MacCoss, M. J., & Moon, R. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1381 · Cited by 364 · see citing works

Building and remodelling Cullin–RING E3 ubiquitin ligases

Lydeard, J. R., Schulman, B. A., & Harper, J. W. (2013) · The EMBO Reports · doi:10.1038/embor.2013.173 · Cited by 327 · see citing works

Iterative Design and Optimization of Initially Inactive Proteolysis Targeting Chimeras (PROTACs) Identify VZ185 as a Potent, Fast, and Selective von Hippel–Lindau (VHL) Based Dual Degrader Probe of BRD9 and BRD7

Zoppi, V., Hughes, S. J., Maniaci, C., Testa, A., Gmaschitz, T., Wieshofer, C., Koegl, M., Riching, K. M., Daniels, D. L., Spallarossa, A., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01413 · Cited by 336 · see citing works

PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

Lo, S.-C., & Hannink, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.02.014 · Cited by 300 · see citing works

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases

Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437996 · Cited by 284 · see citing works

SCFβTrCP-Mediated Degradation of Claspin Regulates Recovery from the DNA Replication Checkpoint Response

Peschiaroli, A., Dorrello, N. V., Guardavaccaro, D., Venere, M., Halazonetis, T., Sherman, N. E., & Pagano, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.013 · Cited by 289 · see citing works

The emerging family of CULLIN3-RING ubiquitin ligases (CRL3s): cellular functions and disease implications

Genschik, P., Sumara, I., & Lechner, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.173 · Cited by 278 · see citing works

CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome.

Groisman, R., Kuraoka, I., Chevallier, O., Gaye, N., Magnaldo, T., Tanaka, K., Kisselev, A. F., Harel-Bellan, A., & Nakatani, Y. (2006) · Genes & Development · doi:10.1101/gad.378206 · Cited by 268 · see citing works

Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins

Pierce, N. W., Lee, J. E., Liu, X., Sweredoski, M. J., Graham, R. L. J., Larimore, E. A., Rome, M., Zheng, N., Clurman, B. E., Hess, S., et al. (2013) · Cell · doi:10.1016/j.cell.2013.02.024 · Cited by 262 · see citing works

Targeting NEDD8-Activated Cullin-RING Ligases for the Treatment of Cancer

Soucy, T. A., Smith, P. G., & Rolfe, M. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-0343 · Cited by 222 · see citing works

Targeting Cullin–RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation

Bulatov, E., & Ciulli, A. (2015) · Biochemical Journal · doi:10.1042/bj20141450 · Cited by 237 · see citing works

Structural assembly of cullin-RING ubiquitin ligase complexes

Zimmerman, E. S., Schulman, B. A., & Zheng, N. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.010 · Cited by 227 · see citing works

The NEDD8 Conjugation Pathway and Its Relevance in Cancer Biology and Therapy

Soucy, T. A., Dick, L. R., Smith, P. G., Milhollen, M. A., & Brownell, J. E. (2010) · Genes & Cancer · doi:10.1177/1947601910382898 · Cited by 225 · see citing works

Lentiviral Vpx Accessory Factor Targets VprBP/DCAF1 Substrate Adaptor for Cullin 4 E3 Ubiquitin Ligase to Enable Macrophage Infection

Srivastava, S., Swanson, S. K., Manel, N., Florens, L., Washburn, M. P., & Skowronski, J. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000059 · Cited by 209 · see citing works

Systematic identification of interactions between host cell proteins and E7 oncoproteins from diverse human papillomaviruses

White, E. A., Sowa, M. E., Tan, M. J. A., Jeudy, S., Hayes, S. D., Santha, S., Münger, K., Harper, J. W., & Howley, P. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116776109 · Cited by 198 · see citing works

Suprafacial Orientation of the SCFCdc4 Dimer Accommodates Multiple Geometries for Substrate Ubiquitination

Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., & Tyers, M. (2007) · Cell · doi:10.1016/j.cell.2007.04.042 · Cited by 209 · see citing works

Structural regulation of cullin-RING ubiquitin ligase complexes

Duda, D. M., Scott, D. C., Calabrese, M. F., Zimmerman, E. S., Zheng, N., & Schulman, B. A. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.01.003 · Cited by 205 · see citing works

PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex

Lo, S.-C., & Hannink, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606539200 · Cited by 199 · see citing works

Characterization of Cullin-box Sequences That Direct Recruitment of Cul2-Rbx1 and Cul5-Rbx2 Modules to Elongin BC-based Ubiquitin Ligases

Mahrour, N., Redwine, W. B., Florens, L., Swanson, S. K., Martin-Brown, S., Bradford, W. D., Staehling-Hampton, K., Washburn, M. P., Conaway, R. C., & Conaway, J. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706987200 · Cited by 196 · see citing works

Chasing molecular glue degraders: screening approaches

Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works

Cell-fate determination by ubiquitin-dependent regulation of translation

Werner, A., Iwasaki, S., McGourty, C. A., Medina-Ruiz, S., Teerikorpi, N., Fedrigo, I., Ingolia, N. T., & Rape, M. (2015) · Nature · doi:10.1038/nature14978 · Cited by 184 · see citing works

The Ubiquitin–Proteasome System in Regulation of the Skeletal Muscle Homeostasis and Atrophy: From Basic Science to Disorders

Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171 · see citing works

Cullin 5 regulates Dab1 protein levels and neuron positioning during cortical development

Feng, L., Allen, N. S., Simo, S., & Cooper, J. A. (2007) · Genes & Development · doi:10.1101/gad.1604207 · Cited by 148 · see citing works

Multiple degradation pathways regulate versatile CIP/KIP CDK inhibitors

Starostina, N. G., & Kipreos, E. T. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.004 · Cited by 147 · see citing works

Highly Selective PTK2 Proteolysis Targeting Chimeras to Probe Focal Adhesion Kinase Scaffolding Functions

Popow, J., Arnhof, H., Bader, G., Berger, H., Ciulli, A., Covini, D., Dank, C., Gmaschitz, T., Greb, P., Karolyi-Özguer, J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01826 · Cited by 138 · see citing works

A Comprehensive Guide to the MAGE Family of Ubiquitin Ligases

Lee, A. K., & Potts, P. R. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.005 · Cited by 136 · see citing works

p63 is a cereblon substrate involved in thalidomide teratogenicity

Asatsuma-Okumura, T., Ando, H., De Simone, M., Yamamoto, J., Sato, T., Shimizu, N., Asakawa, K., Yamaguchi, Y., Ito, T., Guerrini, L., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0366-7 · Cited by 134 · see citing works

L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes

Banks, D., Wu, M., Higa, L. A., Gavrilova, N., Quan, J., Ye, T., Kobayashi, R., Sun, H., & Zhang, H. (2006) · Cell Cycle · doi:10.4161/cc.5.15.3150 · Cited by 127 · see citing works

Functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders

Hanzl, A., Casement, R., Imrichova, H., Hughes, S. J., Barone, E., Testa, A., Bauer, S., Wright, J., Brand, M., Ciulli, A., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-022-01177-2 · Cited by 133 · see citing works

Genome-wide screen identifies cullin-RING ligase machinery required for lenalidomide-dependent CRL4CRBN activity

Sievers, Q. L., Gasser, J. A., Cowley, G. S., Fischer, E. S., & Ebert, B. L. (2018) · Blood · doi:10.1182/blood-2018-01-821769 · Cited by 124 · see citing works

Degradation of Postsynaptic Scaffold GKAP and Regulation of Dendritic Spine Morphology by the TRIM3 Ubiquitin Ligase in Rat Hippocampal Neurons

Hung, A. Y., Sung, C. C., Brito, I. L., & Sheng, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009842 · Cited by 106 · see citing works

Human Immunodeficiency Virus Type 1 Vpr-Binding Protein VprBP, a WD40 Protein Associated with the DDB1-CUL4 E3 Ubiquitin Ligase, Is Essential for DNA Replication and Embryonic Development

McCall, C. M., Miliani de Marval, P. L., Chastain, P. D., Jackson, S. C., He, Y. J., Kotake, Y., Cook, J. G., & Xiong, Y. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00232-08 · Cited by 83 · see citing works

Structural basis of BRCC36 function in DNA repair and immune regulation

Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84 · see citing works

UBE2G1 governs the destruction of cereblon neomorphic substrates

Lu, G., Weng, S., Matyskiela, M., Zheng, X., Fang, W., Wood, S., Surka, C., Mizukoshi, R., Lu, C.-C., Mendy, D., et al. (2018) · eLife · doi:10.7554/elife.40958 · Cited by 78 · see citing works

Enzyme-substrate relationships in the ubiquitin system: approaches for identifying substrates of ubiquitin ligases

O’Connor, H. F., & Huibregtse, J. M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2529-6 · Cited by 42 · see citing works

Sequential replication-coupled destruction at G1/S ensures genome stability

Coleman, K. E., Grant, G. D., Haggerty, R. A., Brantley, K., Shibata, E., Workman, B. D., Dutta, A., Varma, D., Purvis, J. E., & Cook, J. G. (2015) · Genes & Development · doi:10.1101/gad.263731.115 · Cited by 51 · see citing works

NOTCH2 Hajdu-Cheney Mutations Escape SCFFBW7-Dependent Proteolysis to Promote Osteoporosis

Fukushima, H., Shimizu, K., Watahiki, A., Hoshikawa, S., Kosho, T., Oba, D., Sakano, S., Arakaki, M., Yamada, A., Nagashima, K., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.018 · Cited by 46 · see citing works

KLHL39 suppresses colon cancer metastasis by blocking KLHL20-mediated PML and DAPK ubiquitination

Chen, H. Y., Hu, J. Y., Chen, T. H., Lin, Y. C., Liu, X., Lin, M. Y., Lang, Y. D., Yen, Y., & Chen, R. H. (2015) · Oncogene · doi:10.1038/onc.2014.435 · Cited by 39 · see citing works

Structural Basis for Recruitment of DAPK1 to the KLHL20 E3 Ligase

Chen, Z., Picaud, S., Filippakopoulos, P., D'Angiolella, V., & Bullock, A. N. (2019) · Structure · doi:10.1016/j.str.2019.06.005 · Cited by 37 · see citing works

Molecular Architecture of the Ankyrin SOCS Box Family of Cul5-Dependent E3 Ubiquitin Ligases

Muniz, J. R. C., Guo, K., Kershaw, N. J., Ayinampudi, V., von Delft, F., Babon, J. J., & Bullock, A. N. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.06.015 · Cited by 34 · see citing works

Ionizing radiation induces ATM-independent degradation of p21Cip1 in transformed cells

Stuart, S. A., & Wang, J. Y. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808810200 · Cited by 28 · see citing works

Genome-wide CRISPR screens reveal genetic mediators of cereblon modulator toxicity in primary effusion lymphoma

Patil, A., Manzano, M., & Gottwein, E. (2019) · Blood Advances · doi:10.1182/bloodadvances.2019031732 · Cited by 29 · see citing works

Cullin-3–dependent deregulation of ACTN1 represents a pathogenic mechanism in nemaline myopathy

Blondelle, J., Tallapaka, K., Seto, J. T., Ghassemian, M., Clark, M., Laitila, J. M., Bournazos, A., Singer, J. D., & Lange, S. (2019) · JCI Insight · doi:10.1172/jci.insight.125665 · Cited by 26 · see citing works

Evidence for a regulatory role of Cullin-RING E3 ubiquitin ligase 7 in insulin signalling

Scheufele, F., Wolf, B., Kruse, M., et al. (2014) · PMC

Engineering a Ubiquitin Ligase Reveals Conformational Flexibility Required for Ubiquitin Transfer

Qian, S., Wasson, L. K., Choudhary, N. R., Klevit, R. E., Chazin, W., & Patterson, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032334 · Cited by 53 · see citing works

Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C

Paluda, A., Middleton, A. J., Roßig, C., Mace, P. D., & Day, C. L. (2022) · Nature Communications · doi:10.1038/s41467-022-28782-y · Cited by 32 · see citing works

Functional analysis of the ubiquitin ligase Hrd1p with the ubiquitin -conjugating enzyme Ubc7p

Bazirgan, O. A. (2007) · eScholarship (California Digital Library)

Mechanism of Cullin3 E3 Ubiquitin Ligase Dimerization

Choo, Y. Y., & Hagen, T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041350 · Cited by 30 · see citing works